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UniProtKB/Swiss-Prot entry Q05793


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PGBM_MOUSE
Primary accession number Q05793
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 10, 2008 (Entry version 90)
Name and origin of the protein
Protein name Basement membrane-specific heparan sulfate proteoglycan core protein [Precursor]
Synonyms HSPG
Perlecan
PLC
Gene name
Name: Hspg2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Melanoma;
PubMed=1744087 [NCBI, ExPASy, EBI, Israel, Japan]
Noonan D.M., Fulle A., Valente P., Cai S., Horigan E., Sasaki M., Yamada Y., Hassell J.R.;
"The complete sequence of perlecan, a basement membrane heparan sulfate proteoglycan, reveals extensive similarity with laminin A chain, low density lipoprotein-receptor, and the neural cell adhesion molecule.";
J. Biol. Chem. 266:22939-22947(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 940-1601 AND 1870-2600, AND PARTIAL PROTEIN SEQUENCE.
PubMed=2972708 [NCBI, ExPASy, EBI, Israel, Japan]
Noonan D.M., Horigan E.A., Ledbetter S.R., Vogeli G., Sasaki M., Yamada Y., Hassell J.R.;
"Identification of cDNA clones encoding different domains of the basement membrane heparan sulfate proteoglycan.";
J. Biol. Chem. 263:16379-16387(1988).
[3]
PARTIAL PROTEIN SEQUENCE.
PubMed=7649154 [NCBI, ExPASy, EBI, Israel, Japan]
Schulze B., Mann K., Battistutta R., Wiedemann H., Timpl R.;
"Structural properties of recombinant domain III-3 of perlecan containing a globular domain inserted into an epidermal-growth-factor-like motif.";
Eur. J. Biochem. 231:551-556(1995).
[4]
INTERACTION WITH VWA1.
DOI=10.1074/jbc.M513746200; PubMed=16407285 [NCBI, ExPASy, EBI, Israel, Japan]
Allen J.M., Bateman J.F., Hansen U., Wilson R., Bruckner P., Owens R.T., Sasaki T., Timpl R., Fitzgerald J.;
"WARP is a novel multimeric component of the chondrocyte pericellular matrix that interacts with perlecan.";
J. Biol. Chem. 281:7341-7349(2006).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1761-1858 IN COMPLEX WITH A NIDOGEN FRAGMENT.
DOI=10.1038/89683; PubMed=11427896 [NCBI, ExPASy, EBI, Israel, Japan]
Hopf M., Gohring W., Ries A., Timpl R., Hohenester E.;
"Crystal structure and mutational analysis of a perlecan-binding fragment of nidogen-1.";
Nat. Struct. Biol. 8:634-640(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M77174; AAA39911.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04054; AAA39899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J04055; AAA39912.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S18252; S18252.
UniGene Mm.273662
3D structure databases
PDB
1GL4; X-ray; 2.00 A; B=1765-1858.[ExPASy / RCSB / EBI]
PDBsum 1GL4; -.
ModBase Q05793.
Protein-protein interaction databases
IntAct Q05793; -.
Organism-specific databases
MGI MGI:96257; Hspg2.
GeneLynx Hspg2; Mus musculus.
Gene expression databases
CleanEx MM_HSPG2; -.
GermOnline ENSMUSG00000028763; Mus musculus.
Ontologies
GO
GO:0005604; Cellular component: basement membrane (inferred from direct assay from MGI).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0008104; Biological process: protein localization (inferred from mutant phenotype from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013320; ConA_like_subgrp.
IPR006210; EGF.
IPR000742; EGF_3.
IPR002049; EGF_laminin.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003599; Ig_sub.
IPR003598; Ig_sub2.
IPR013106; Ig_V-set.
IPR000034; Laminin_B.
IPR001791; Laminin_G.
IPR012680; Laminin_G_2.
IPR002172; LDL_rcpt_classA_cys-rich.
IPR000082; SEA.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.200; ConA_like_subgrp; 3.
G3DSA:2.60.40.10; Ig-like_fold; 14.
G3DSA:4.10.400.10; LDL_rcpt_classA_cys-rich; 3.
Pfam PF00008; EGF; 3.
PF07679; I-set; 9.
PF00047; ig; 5.
PF00052; Laminin_B; 3.
PF00053; Laminin_EGF; 8.
PF02210; Laminin_G_2; 3.
PF00057; Ldl_recept_a; 4.
PF01390; SEA; 1.
PF07686; V-set; 1.
Pfam graphical view of domain structure.
PRINTS PR00261; LDLRECEPTOR.
ProDom PD003031; Laminin_B; 3.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00181; EGF; 3.
SM00180; EGF_Lam; 7.
SM00409; IG; 1.
SM00408; IGc2; 14.
SM00281; LamB; 3.
SM00282; LamG; 3.
SM00192; LDLa; 4.
SM00200; SEA; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; 8.
PS01186; EGF_2; 5.
PS50026; EGF_3; 4.
PS01248; EGF_LAM_1; 11.
PS50027; EGF_LAM_2; 8.
PS50835; IG_LIKE; 15.
PS50025; LAM_G_DOMAIN; 3.
PS51115; LAMININ_IVA; 3.
PS01209; LDLRA_1; 4.
PS50068; LDLRA_2; 4.
PS50024; SEA; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q05793.
Genome annotation databases
Ensembl ENSMUSG00000028763; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM Q05793; -.
HOVERGEN Q05793; -.
Other
SOURCE Hspg2; Mus musculus.
ProtoNet Q05793.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Basement membrane; Direct protein sequencing; EGF-like domain; Extracellular matrix; Glycoprotein; Heparan sulfate; Immunoglobulin domain; Laminin EGF-like domain; Proteoglycan; Repeat; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     21  21     Potential. 
CHAIN   22   3707  3686     Basement membrane-specific heparan sulfate proteoglycan core protein. PRO_0000026697
DOMAIN   80    194  115     SEA. 
DOMAIN   195    234  40     LDL-receptor class A 1. 
DOMAIN   281    319  39     LDL-receptor class A 2. 
DOMAIN   320    359  40     LDL-receptor class A 3. 
DOMAIN   360    403  44     LDL-receptor class A 4. 
DOMAIN   404    504  101     Ig-like C2-type 1. 
DOMAIN   521    530  10     Laminin EGF-like 1; first part. 
DOMAIN   538    730  193     Laminin IV type A 1. 
DOMAIN   731    763  33     Laminin EGF-like 1; second part. 
DOMAIN   764    813  50     Laminin EGF-like 2. 
DOMAIN   814    871  58     Laminin EGF-like 3. 
DOMAIN   879    923  45     Laminin EGF-like 4; truncated. 
DOMAIN   924    933  10     Laminin EGF-like 5; first part. 
DOMAIN   941   1125  185     Laminin IV type A 2. 
DOMAIN   1126   1158  33     Laminin EGF-like 5; second part. 
DOMAIN   1159   1208  50     Laminin EGF-like 6. 
DOMAIN   1209   1265  57     Laminin EGF-like 7. 
DOMAIN   1275   1324  50     Laminin EGF-like 8. 
DOMAIN   1325   1334  10     Laminin EGF-like 9; first part. 
DOMAIN   1344   1529  186     Laminin IV type A 3. 
DOMAIN   1530   1562  33     Laminin EGF-like 9; second part. 
DOMAIN   1563   1612  50     Laminin EGF-like 10. 
DOMAIN   1613   1670  58     Laminin EGF-like 11. 
DOMAIN   1677   1771  95     Ig-like C2-type 2. 
DOMAIN   1772   1865  94     Ig-like C2-type 3. 
DOMAIN   1866   1954  89     Ig-like C2-type 4. 
DOMAIN   1955   2049  95     Ig-like C2-type 5. 
DOMAIN   2050   2148  99     Ig-like C2-type 6. 
DOMAIN   2149   2244  96     Ig-like C2-type 7. 
DOMAIN   2245   2343  99     Ig-like C2-type 8. 
DOMAIN   2344   2436  93     Ig-like C2-type 9. 
DOMAIN   2437   2532  96     Ig-like C2-type 10. 
DOMAIN   2533   2619  87     Ig-like C2-type 11. 
DOMAIN   2620   2720  101     Ig-like C2-type 12. 
DOMAIN   2721   2809  89     Ig-like C2-type 13. 
DOMAIN   2810   2895  86     Ig-like C2-type 14. 
DOMAIN   2896   2980  85     Ig-like C2-type 15. 
DOMAIN   2984   3162  179     Laminin G-like 1. 
DOMAIN   3163   3241  79     EGF-like. 
DOMAIN   3245   3425  181     Laminin G-like 2. 
DOMAIN   3518   3705  188     Laminin G-like 3. 
REGION   3615   3617  3     Mediates motor neuron attachment (Potential). 
CARBOHYD   65     65        O-linked (Xyl...) (heparan sulfate) (Potential). 
CARBOHYD   71     71        O-linked (Xyl...) (heparan sulfate) (Potential). 
CARBOHYD   76     76        O-linked (Xyl...) (heparan sulfate) (Potential). 
CARBOHYD   89     89        N-linked (GlcNAc...) (Potential). 
CARBOHYD   358    358        N-linked (GlcNAc...) (Potential). 
CARBOHYD   554    554        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1256   1256        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1891   1891        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2336   2336        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2394   2394        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2427   2427        N-linked (GlcNAc...) (Potential). 
CARBOHYD   2600   2600        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3098   3098        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3154   3154        N-linked (GlcNAc...) (Potential). 
CARBOHYD   3385   3385        N-linked (GlcNAc...) (Potential). 
DISULFID   199    212        By similarity. 
DISULFID   206    225        By similarity. 
DISULFID   219    234        By similarity. 
DISULFID   285    297        By similarity. 
DISULFID   292    310        By similarity. 
DISULFID   304    319        By similarity. 
DISULFID   325    337        By similarity. 
DISULFID   332    350        By similarity. 
DISULFID   344    359        By similarity. 
DISULFID   368    381        By similarity. 
DISULFID   375    394        By similarity. 
DISULFID   388    403        By similarity. 
DISULFID   428    479        By similarity. 
DISULFID   764    773        By similarity. 
DISULFID   766    780        By similarity. 
DISULFID   783    792        By similarity. 
DISULFID   795    811        By similarity. 
DISULFID   814    829        By similarity. 
DISULFID   816    839        By similarity. 
DISULFID   842    851        By similarity. 
DISULFID   854    869        By similarity. 
DISULFID   879    892        By similarity. 
DISULFID   894    903        By similarity. 
DISULFID   906    921        By similarity. 
DISULFID   1159   1168        By similarity. 
DISULFID   1161   1175        By similarity. 
DISULFID   1178   1187        By similarity. 
DISULFID   1190   1206        By similarity. 
DISULFID   1209   1224        By similarity. 
DISULFID   1211   1234        By similarity. 
DISULFID   1237   1246        By similarity. 
DISULFID   1249   1263        By similarity. 
DISULFID   1275   1287        By similarity. 
DISULFID   1277   1293        By similarity. 
DISULFID   1295   1304        By similarity. 
DISULFID   1307   1322        By similarity. 
DISULFID   1563   1572        By similarity. 
DISULFID   1565   1579        By similarity. 
DISULFID   1582   1591        By similarity. 
DISULFID   1594   1610        By similarity. 
DISULFID   1613   1628        By similarity. 
DISULFID   1615   1638